accession
stringlengths
6
10
name
stringlengths
6
11
Full Name
stringlengths
1
147
taxon
stringlengths
3
46
sequence
stringlengths
16
2.75k
function
stringlengths
6
5.51k
AlphaFoldDB
stringlengths
6
10
O76064
RNF8_HUMAN
RING-type E3 ubiquitin transferase RNF8
Homo
MGEPGFFVTGDRAGGRSWCLRRVGMSAGWLLLEDGCEVTVGRGFGVTYQLVSKICPLMISRNHCVLKQNPEGQWTIMDNKSLNGVWLNRARLEPLRVYSIHQGDYIQLGVPLENKENAEYEYEVTEEDWETIYPCLSPKNDQMIEKNKELRTKRKFSLDELAGPGAEGPSNLKSKINKVSCESGQPVKSQGKGEVASTPSDNLDPKLTALEPSKTTGAPIYPGFPKVTEVHHEQKASNSSASQRSLQMFKVTMSRILRLKIQMQEKHEAVMNVKKQTQKGNSKKVVQMEQELQDLQSQLCAEQAQQQARVEQLEKTFQEEEQHLQGLEIAQGEKDLKQQLAQALQEHWALMEELNRSKKDFEAIIQAKNKELEQTKEEKEKMQAQKEEVLSHMNDVLENELQCIICSEYFIEAVTLNCAHSFCSYCINEWMKRKIECPICRKDIKSKTYSLVLDNCINKMVNNLSSEVKERRIVLIRERKAKRLF
E3 ubiquitin-protein ligase that plays a key role in DNA damage signaling via 2 distinct roles: by mediating the 'Lys-63'-linked ubiquitination of histones H2A and H2AX and promoting the recruitment of DNA repair proteins at double-strand breaks (DSBs) sites, and by catalyzing 'Lys-48'-linked ubiquitination to remove target proteins from DNA damage sites. Following DNA DSBs, it is recruited to the sites of damage by ATM-phosphorylated MDC1 and catalyzes the 'Lys-63'-linked ubiquitination of histones H2A and H2AX, thereby promoting the formation of TP53BP1 and BRCA1 ionizing radiation-induced foci (IRIF). Also controls the recruitment of UIMC1-BRCC3 (RAP80-BRCC36) and PAXIP1/PTIP to DNA damage sites. Also recruited at DNA interstrand cross-links (ICLs) sites and catalyzes 'Lys-63'-linked ubiquitination of histones H2A and H2AX, leading to recruitment of FAAP20/C1orf86 and Fanconi anemia (FA) complex, followed by interstrand cross-link repair. H2A ubiquitination also mediates the ATM-dependent transcriptional silencing at regions flanking DSBs in cis, a mechanism to avoid collision between transcription and repair intermediates. Promotes the formation of 'Lys-63'-linked polyubiquitin chains via interactions with the specific ubiquitin-conjugating UBE2N/UBC13 and ubiquitinates non-histone substrates such as PCNA. Substrates that are polyubiquitinated at 'Lys-63' are usually not targeted for degradation. Also catalyzes the formation of 'Lys-48'-linked polyubiquitin chains via interaction with the ubiquitin-conjugating UBE2L6/UBCH8, leading to degradation of substrate proteins such as CHEK2, JMJD2A/KDM4A and KU80/XRCC5: it is still unclear how the preference toward 'Lys-48'- versus 'Lys-63'-linked ubiquitination is regulated but it could be due to RNF8 ability to interact with specific E2 specific ligases. For instance, interaction with phosphorylated HERC2 promotes the association between RNF8 and UBE2N/UBC13 and favors the specific formation of 'Lys-63'-linked ubiquitin chains. Promotes non-homologous end joining (NHEJ) by promoting the 'Lys-48'-linked ubiquitination and degradation the of KU80/XRCC5. Following DNA damage, mediates the ubiquitination and degradation of JMJD2A/KDM4A in collaboration with RNF168, leading to unmask H4K20me2 mark and promote the recruitment of TP53BP1 at DNA damage sites . Following DNA damage, mediates the ubiquitination and degradation of POLD4/p12, a subunit of DNA polymerase delta. In the absence of POLD4, DNA polymerase delta complex exhibits higher proofreading activity . In addition to its function in damage signaling, also plays a role in higher-order chromatin structure by mediating extensive chromatin decondensation. Involved in the activation of ATM by promoting histone H2B ubiquitination, which indirectly triggers histone H4 'Lys-16' acetylation (H4K16ac), establishing a chromatin environment that promotes efficient activation of ATM kinase. Required in the testis, where it plays a role in the replacement of histones during spermatogenesis. At uncapped telomeres, promotes the joining of deprotected chromosome ends by inducing H2A ubiquitination and TP53BP1 recruitment, suggesting that it may enhance cancer development by aggravating telomere-induced genome instability in case of telomeric crisis. Promotes the assembly of RAD51 at DNA DSBs in the absence of BRCA1 and TP53BP1 Also involved in class switch recombination in immune system, via its role in regulation of DSBs repair. May be required for proper exit from mitosis after spindle checkpoint activation and may regulate cytokinesis. May play a role in the regulation of RXRA-mediated transcriptional activity. Not involved in RXRA ubiquitination by UBE2E2 .
O76064
Q0ZIZ0
PSBH_VITVI
Photosystem II 10 kDa phosphoprotein
Vitis
MATKTVEGSSRSRPKPTTVGELLKPLNSEYGKVAPGWGTTPLMGVAMALFAVFLSIILEIYNSSVLLDGISLN
One of the components of the core complex of photosystem II (PSII), required for its stability and/or assembly. PSII is a light-driven water:plastoquinone oxidoreductase that uses light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient subsequently used for ATP formation. It consists of a core antenna complex that captures photons, and an electron transfer chain that converts photonic excitation into a charge separation.
Q0ZIZ0
P0DM69
TX5_SELPU
Toxin OAIP 5
Selenotypus
MLIVILTCALLVIYHAAAAEELEAKDVIESKALATLDEERFECVLKCDIQYNGKNCKGKGENKCSGGWRCRFKLCLKI
Probable ion channel inhibitor. Shows insecticidal activity when injected into mealworms.
P0DM69
A3QAD1
PSD_SHELP
Phosphatidylserine decarboxylase beta chain
Shewanella
MDKLKIALQYIMPKHLLSRLVGKLAAAELGAVTTSVIKWFIKQYKIDMSEAAQSAPEAYASFNQFFTRALKPGIRPLCDDDDYIVHPVDGAVSQCGPIKEGRIFQAKGHEYSSLALLGDQADDAKRFEGGDFATIYLAPKDYHRIHMPIKGTLSKMTYVPGELFSVNPLTAENVPGLFARNERVVAIFETEIGPMAMVLVGATIVASIETVWAGTVTPPTGKKVFTWDYPTEGPEAITLDKGEEMGRFKLGSTVVMLFAKDALEHFADGVEPKAVTRMGQAFAKID
Catalyzes the formation of phosphatidylethanolamine (PtdEtn) from phosphatidylserine (PtdSer).
A3QAD1
P14498
TRAS2_ECOLX
Protein TraS
Escherichia
MKRSDLEKDAAYILDKFKQLDYEIPSNRQILKVIFYKLVVVYVFQLLFIIFDIFINSNVRDYHYFDTFVITLGSNAFFSLVFLMSTYNLVSLKISLGSEITEQSVLLKLVERKINSYGQFLMVVNAIVGCVLLSSGERFVAGLGFSWFVTYLISMITLQTSLSRYMTPAVVSSLSKVKELLSASPK
Involved in surface exclusion.
P14498
C0HKD6
SYWM_CAEEL
Tryptophanyl-tRNA synthetase
Caenorhabditis
MIFSGKFTSHLLNYGFKPNNLRLLSTSTHPTIYFTGIQPTGIPHLGNFFGSIEPWTELQNSVDKNILMMLSVVDQHAISLGPLPANELRQNTHQMTASLIACGVDPNRTLLFRQSDVPQIAQISWILGSLQTTSKLARLPQYKEKKERFKKGDIPVGLLTYPLLQAADVLTFKATTVPVGEDQSQHLNLLGGLAYAFNKTYETEIFPIPKQLTRESHARIRSLREPEKKMSKSSGGPRSRIEITDSRSTIIEKCQKAQSDNAGKVTYDKENRLAVSNLLDLYSAVTKTQTSEIDFSNWTTLDLKMNLAEAVDKRLAPIRQKFEELQNTGEVDKVLTENGEKAREIAEKNLEEIRRTIGFL
Catalyzes the attachment of tryptophan to tRNA(Trp).
C0HKD6
Q62918
NELL2_RAT
NEL-like protein 2
Rattus
MESRVLLRTFCVILGLEAVWGLGVDPSLQIDVLSELELGESTAGVRQVPGLHNGTKAFLFQDSPRSIKAPIATAERFFQKLRNKHEFTILVTLKQIHLNSGVILSIHHLDHRYLELESSGHRNEIRLHYRSGTHRPHTEVFPYILADAKWHKLSLAFSASHLILHIDCNKIYERVVEMPSTDLPLGTTFWLGQRNNAHGYFKGIMQDVQLLVMPQGFIAQCPDLNRTCPTCNDFHGLVQKIMELQDILSKTSAKLSRAEQRMNRLDQCYCERTCTMKGATYREFESWTDGCKNCTCLNGTIQCETLVCPAPDCPAKSAPAYVDGKCCKECKSTCQFQGRSYFEGERSTVFSASGMCVLYECKDQTMKLVENAGCPALDCPESHQIALSHSCCKVCKGYDFCSEKHTCMENSVCRNLNDRAVCSCRDGFRALREDNAYCEDIDECAEGRHYCRENTMCVNTPGSFLCICQTGYIRIDDYSCTEHDECLTNQHNCDENALCFNTVGGHNCVCKPGYTGNGTTCKAFCKDGCKNGGACIAANVCACPQGFTGPSCETDIDECSEGFVQCDSRANCINLPGWYHCECRDGYHDNGMFAPGGESCEDIDECGTGRHSCANDTICFNLDGGYDCRCPHGKNCTGDCVHDGKVKHNGQIWVLENDRCSVCSCQTGFVMCQRMVCDCENPTVDLSCCPECDPRLSSQCLHQNGETVYNSGDTWAQDCRQCRCLQEEVDCWPLACPEVECEFSVLPENECCPRCVTDPCQADTIRNDITKTCLDEMNVVRFTGSSWIKHGTECTLCQCKNGHVCCSVDPQCLQEL
Required for neuron survival through the modulation of MAPK pathways . Involved in the regulation of hypothalamic GNRH secretion and the control of puberty.
Q62918
P68030
HBG_ALOBE
Hemoglobin gamma chain
Alouatta
MSNFTAEDKAAITSLWGKVNVEDAGGETLGRLLVVYPWTQRFFDSFGSLSSPSAIMGNPKVKAHGVKVLTSLGEAIKNLDDLKGTFGSLSELHCDKLHVDPENFRLLGNVLVTVLAILHGKEFTPEVQASWQKMVAGVASALASRYH
Gamma chains make up the fetal hemoglobin F, in combination with alpha chains.
P68030
A7H3F3
ISPH_CAMJD
4-hydroxy-3-methylbut-2-enyl diphosphate reductase
Campylobacter
MIIELAKNYGFCFGVKRAIKKAEQIKDAATIGPLIHNNEEISRLQKNFNVKTLENIKSLSNETKAIIRTHGITKQDLEELRKKDIEIFDATCPFVTKPQQICEQMSKEGYEIVIFGDENHPEVKGVKSYVNTKAYVVLDKKELQNIKLPSKIAVVSQTTKKPEHFMEIVNFLMLKAKEVRVFNTICDATFKNQDAIKELSLKSDVMVVVGGKNSANTKQLFLIAKTNCEDSYLIETEEELKKEWFLDKKHCGISAGASTPDWIIQKVIAKIENFGIN
Catalyzes the conversion of 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate (HMBPP) into a mixture of isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP). Acts in the terminal step of the DOXP/MEP pathway for isoprenoid precursor biosynthesis.
A7H3F3
P20784
ROL6_CAEEL
Protein roller-6
Caenorhabditis
MTLTTATSGAIVFSGATLLVSLFAAASLYSQVSNIWNELDAEIANFRSLTEDMWVDMVKLGAGTASNRVRRQQYGGYGATGVQPPAPTPNPYGGYGASQPAPPEKFPDGIPNGGNQPKFPGGGFPDGPFPNGGGPRGGNQCQCTVENSCPPGPAGPEGEEGPDGHDGQDGVPGFDGKDAEDVQNTPPTGCFTCPQGPLGPQGPNGAPGLRGMRGARGQPGRPGRDGNPGMPGDCGPPGAPGSDGKPGSPGGKGDDGERPLGRPGPRGPPGEAGPEGPQGPTGRDAYPGQSGPQGEPGLQGYGGAAGEDGPEGPPGAPGLPGKDAEYCKCPGREGDAGRSARRHRKFQL
Nematode cuticles are composed largely of collagen-like proteins. The cuticle functions both as an exoskeleton and as a barrier to protect the worm from its environment. Involved in body morphogenesis .
P20784
Q96EY5
MB12A_HUMAN
Protein FAM125A
Homo
MDPVPGTDSAPLAGLAWSSASAPPPRGFSAISCTVEGAPASFGKSFAQKSGYFLCLSSLGSLENPQENVVADIQIVVDKSPLPLGFSPVCDPMDSKASVSKKKRMCVKLLPLGATDTAVFDVRLSGKTKTVPGYLRIGDMGGFAIWCKKAKAPRPVPKPRGLSRDMQGLSLDAASQPSKGGLLERTASRLGSRASTLRRNDSIYEASSLYGISAMDGVPFTLHPRFEGKSCSPLAFSAFGDLTIKSLADIEEEYNYGFVVEKTAAARLPPSVS
Component of the ESCRT-I complex, a regulator of vesicular trafficking process. Required for the sorting of endocytic ubiquitinated cargos into multivesicular bodies. May be involved in the ligand-mediated internalization and down-regulation of EGF receptor.
Q96EY5
A6MM38
RR4_BUXMI
30S ribosomal protein S4, chloroplastic
Buxus
MSRYRGPRFKKIRRLGALPGLTSKRPRAGSDLRNQSRSGKRSQYRIRLEEKQKLRFHYGLTERQLLKYVRIAGKAKGSTGQVLLQLLEMRLDNILFRLGMASTIPGARQLVNHRHILVNGRIVDIPSYRCKPRDIITAKDEQKSRALIQNYLDSSPHEELPKHLTLHSFQYKGLVNQIIDSKWVGLKINELLVVEYYSRQT
With S5 and S12 plays an important role in translational accuracy.
A6MM38
A1S3W8
TYSY_SHEAM
Thymidylate synthase
Shewanella
MKQYLDLMKHILDKGTDKSDRTGTGTRSVFGYQMRFDLNEGFPLVTTKKCHLRSIIHELLWFLKGETNVDYLHENKVSIWDEWADEKGNLGPVYGAQWRSWPTPDGRHIDQISQVIEQIKATPDSRRLIVSAWNVGELDKMALAPCHAFFQFYVADGKLSCQLYQRSCDVFLGLPFNIASYALLTMMVAQQCNLGLGDFVWTGGDTHLYSNHMEQTQLQLSREPRPLPTMKILRHPESIFDYRFEDFELSGYDPHPHIKAPVAI
Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis.
A1S3W8
P59558
RL22_BUCBP
50S ribosomal protein L22
Buchnera
METIARHSQARSSAQKLRLVADLIRGKNIEHALNILTFCNKKASILVKKVLKSAISNAEHNHGSDINNLQVKKILIDEGPTMKRMMPRAKGRSDRILKRTSHITIVVSDSKVKDKKGRG
The globular domain of the protein is located near the polypeptide exit tunnel on the outside of the subunit, while an extended beta-hairpin is found that lines the wall of the exit tunnel in the center of the 70S ribosome.
P59558
C3JZP4
RBSD_PSEFS
D-ribose pyranase
Pseudomonas
MKKTPLLNIALSRVIASLGHGDILVIGDAGLPVPPGVELIDLALTQGIPDFISALRIVLSEMQVESHVLAEEILLKQPPALNELNTLSDEAALGERRLVSHEAFKQLSRKARAVVRTGECQPYCNIALVSGVTF
Catalyzes the interconversion of beta-pyran and beta-furan forms of D-ribose.
C3JZP4
B8D9D7
ACP_BUCA5
Acyl carrier protein
Buchnera
MKNIEERIKKIIFEKLDIKQEKIFNDASFIDDLGADSLDTVELIMALEEEFDIEISDEEAEKINTVQKSIDFIQNKNLKK
Carrier of the growing fatty acid chain in fatty acid biosynthesis.
B8D9D7
Q8R3I2
MBOA2_MOUSE
Membrane-bound O-acyltransferase domain-containing protein 2
Mus
MATTSTTGSTLLQPLSNAVQLPIDQVNFVVCQLFALLAAVWFRTYLHSSKTSSFIRHVVATLLGLYLAFFCFGWYALHFLVQSGISYCIMIIAGVESMQQCCFVFALGYLSVCQITRVYIFDYGQYSADFSGPMMIITQKITSLAYEIHDGMFRKDEELTPSQRGLAVRRMPSLLEYVSYTCNFMGILAGPLCSYKDYIAFIEGRASHVAQPSENGKDEQHGKADPSPNAAVTEKLLVCGLSLLFHLTISNMLPVEYNIDEHFQATASWPTKATYLYVSLLAARPKYYFAWTLADAINNAAGFGFRGYDKNGVARWDLISNLRIQQIEMSTSFKMFLDNWNIQTALWLKRVCYERATFSPTIQTFFLSAIWHGVYPGYYLTFLTGVLMTLAARAVRNNFRHYFLEPPQLKLFYDLITWVATQITISYTVVPFVLLSIKPSFTFYSSWYYCLHVCSILVLLLLPVKKSQRRTSTQENVHLSQAKKFDERDNPLGQNSFSTMNNVCNQNRDTGSRHSSLTQ
Acyltransferase which catalyzes the transfert of an acyl group from an acyl-CoA to a lysophospholipid leading to the production of a phospholipid and participates in the reacylation step of the phospholipid remodeling pathway also known as the Lands cycle . Catalyzes the acylation of lysophosphatidylcholine (1-acyl-sn-glycero-3-phosphocholine or LPC) and to a lesser extend lysophosphatidylethanolamine (1-acyl-sn-glycero-3-phosphoethanolamine or LPE) . Does not acylates lysophosphatidic acid (LPA) and lysophosphatidylserine . Prefers oleoyl-CoA as the acyl donor . May be involved in chondrocyte differentiation .
Q8R3I2
Q3K5C0
MDCG_PSEPF
Malonate decarboxylase holo-[acyl-carrier-protein] synthase
Pseudomonas
MVNTPLAHDLLWGMTPAQLPADAPQWAIDSLAAGQPVVVRRALSEDGCVAVGVRGRFREQRLAAFMSVDSIACRVSPEALCQVESARDLPVMQALRQLRPVLDDCGWTWGVSGSVGFELASGFTAMHERSDLDLILRTPQLITRNQARKLVAYFEQAICRVDLQLQTPFGAVALREWAGNASRVLLKNAREACLVSDPWNPQEQAA
Transfers 2'-(5-triphosphoribosyl)-3'-dephosphocoenzyme-A to the apo-[acyl-carrier-protein] of the malonate decarboxylase to yield holo-[acyl-carrier-protein].
Q3K5C0
B1VAN0
RL11_PHYAS
50S ribosomal protein L11
16SrXII (Stolbur group)
MAKKVVKMVKLQIPAGKANPAPPVGPALGQAQVNIPSFCSQFNETTKDQMGFIIPVIISVYEDRTFTFVTKTPPASDLLKKAAKIDAGSANAKQTKVATISKSQLQEIANLKLRDLNAYSVEQACKIIAGTARNMGILIED
Forms part of the ribosomal stalk which helps the ribosome interact with GTP-bound translation factors.
B1VAN0
B7HPL5
HRCA_BACC7
Heat-inducible transcription repressor HrcA
Bacillus cereus group
MLTERQLLILQTIIDDFIGSAQPVGSRTLAKKDEITFSSATIRNEMADLEELGFIEKTHSSSGRVPSEKGYRFYVDHLLAPQNLPNDEIVQIKDLFAERIFEAEKIAQQSAQILSELTNYTAIVLGPKLSTNKLKNVQIVPLDRQTAVAIIVTDTGHVQSKTITVPESVDLSDLEKMVNILNEKLSGVPMSELHNKIFKEIVTVLRGYVHNYDSAIKILDGTFQVPLSEKIYFGGKANMLSQPEFHDIQKVRSLLTMIDNEAEFYDILRHKQVGIQVKIGRENSATAMEDCSLISATYSIGEEQLGTIAILGPTRMQYSRVISLLQLFTRQITDGLKK
Negative regulator of class I heat shock genes (grpE-dnaK-dnaJ and groELS operons). Prevents heat-shock induction of these operons.
B7HPL5
P73451
NRTB_SYNY3
Nitrate import permease protein NrtB
unclassified Synechocystis
MASSTAGLRPRRKKNPLSFIYSPKVIRPAVAIAVLLVVWQILCSGEGSNLPSPVQVLEQTYPLILNPFFDNGGTDKGLGIQIFASLTRVAVGFSAAAVVGIALGILIGSSKFMYDALDPIFQVLRTIPPLAWLPIALAALQEAEPSAIFVIFITAIWPIVINTTVGAQQVPQDYRNVSRVLKLSKSQYFFNILFPAAVPYIFTGLRIGIGLSWLAIVAAEMLIGGVGIGFFIWDAYNSSLISEIIIALIYVGIVGLLLDRFIAFLESLVVPAEQK
Part of the ABC transporter complex NrtABCD involved in nitrate uptake. The complex is probably also involved in nitrite transport. Probably responsible for the translocation of the substrate across the membrane.
P73451
Q8PII0
YQGF_XANAC
Putative pre-16S rRNA nuclease
Xanthomonas
MPEAGAIRPDGTVLGFDVGSRRIGVAVGSALGAGARAVAVINVHANGPDWVALDRVHKQWRPDGLVVGDPLTLDDKDQPARKRAHAFARQLRERYALPVVLIDERSSSVEAAQRFARERADGRKRRRDAEALDAMAAAVIVERWLAAPDQATLLP
Could be a nuclease involved in processing of the 5'-end of pre-16S rRNA.
Q8PII0
A7GS30
METE_BACCN
Methionine synthase, vitamin-B12 independent isozyme
Bacillus cereus group
MALHTSNLGYPRIGLQREWKKTLEAFWAQKIDEQQLITTMKEIHLEHLNVQKEKGIDFIPIGDFTYYDHVLDTAYMLGFIPSRFSNFTSYLDIYFAMARGSKDHVASEMTKWFNTNYHYIVPEYEEGLNISLKDNRPLRLYEEAKRELGIDGKPVILGPYTFLKLAKGYTQDQFPTILHKLIAPYVQLLTELHKAGARLIQIDEPIFVSLTKEEMIEAKKLYEAIQKEVPSANLILQTYFDSVEENYTELITFPVSGIGLDFVHGKEGNIKSIVEHGFPAEKTLAIGCIDGRNIWRANLDEVFALFETLKAHIEPKDWIIQPSCSLLHTPVDKTEETHLSPELFDALAFANQKLEELTLIKRGLSEGVNSIEIEITTYRNSHEAVRSSAARNRKDVQTARASLKEEDFSRPLPFEQRYDLQQKALQLPLLPTTTIGSFPQTPEVRQTRKQWRNGEITNEQYEHFIEQETEKWIRHQENIGLDVLVHGEFERTDMVEYFGERLAGFSFTKNGWVQSYGSRCVKPPIIFGDVAFISDMTVKETVYAQSLTNKVVKGMLTGPVTILNWSFVRNDLPRKEVCYQIALALRHEIERLESSGIRIIQVDEPALREGMPLKEKDWDSYIEWAVQSFRLATASVANETQIHTHMCYSNFEDIVDAIRALDADVISIETSRSHGEFIHTLEQTTYEKGIGLGVYDIHSPRVPSKEEMYTIVEQSLKVCNPKYFWINPDCGLKTRRTEEVLPALEHMVEAAKEARTLLKTNA
Catalyzes the transfer of a methyl group from 5-methyltetrahydrofolate to homocysteine resulting in methionine formation.
A7GS30
O06431
DNAJ_NITEU
Chaperone protein DnaJ
Nitrosomonas
MSQSDYYEVLGVGRDADENELKKAYRKLAMKYHPDRNAGDTKAEERFKNIKEAYEILSDPNKRAAYDQFGHAGLNGGMGGAGAQGFSDAFSDIFSDLFGMRGGGRSSVHRGADLRYNLEITLEQAARGAETQIRIPRQEVCDTCHGSGAKPGTSPKTCPTCNGHGQIRMQQGFFSIQQTCSHCQGSGKVVSDPCGDCHGAGWVKRQKTLSVRIPAGVDEGDSIRLTGEGEAGANGGQAGDLYIVIHLASHPVFQREGNHLHCEIPISFTVAALGGEIEVPTLDGHARIKVPAGTQTGKIFRLRSKGITGVRNQSTGDLLCHVAVETPVDLTARQKELLEEFESISQKDGSRHHPRAKSWMEKAREFFAE
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
O06431
B0BTY6
HFQ_ACTPJ
RNA-binding protein Hfq
Actinobacillus
MAKGQSLQDPYLNALRRERIPVSIYLVNGIKLQGQIESFDQFVILLKNTVSQMVYKHAISTVVPARSVSHNNGGAAHTQQSPAVEAVADKAE
RNA chaperone that binds small regulatory RNA (sRNAs) and mRNAs to facilitate mRNA translational regulation in response to envelope stress, environmental stress and changes in metabolite concentrations. Also binds with high specificity to tRNAs.
B0BTY6
C4LC89
TRPB_TOLAT
Tryptophan synthase beta chain
Tolumonas
MTLLDPFFGEFGGMYSPQILMPVLLELEKAFVDAKDDPEFQAEFQHLLTEYAGRPTPLTLCRNLTKGTKTKIYLKREDLLHGGAHKTNQVLGQALLAKRMGKTRIIAETGAGQHGVATALACALLDLPCRIYMGAVDCERQKPNVFRMRLMGAEVIPVHAGSSTLKDACNEAMRDWTANYKDTHYILGTAAGPHPFPTIVREFQRMIGEEAKEQILKAEGRLPDAVVACVGGGSNAIGMFATFIEEEGVRLIGVEPAGHGIETGKHGAPIGHARKGIYLGMVSFLMQNEDGQVEESHSISAGLDFPSVGPQHAYLSSIGRAQYPSVTDQEALDAFQELSLREGIIPALESSHALAHALKMARSEPEKEQILIVNLSGRGDKDIFTVANALEGEGALS
The beta subunit is responsible for the synthesis of L-tryptophan from indole and L-serine.
C4LC89
B7UWI1
HSCA_PSEA8
Chaperone protein HscA homolog
Pseudomonas
MALLQIAEPGQSPKPHERRLAVGIDLGTTNSLVAAVRSGVAEPLPDAQGRLILPSAVRYHAERAEVGESARAAAAEDPFNTVISVKRLMGRGLEDVKQLGEQLPYRFRQGESHMPFIETVQGLKSPVEVSADILRELRQRAETTLGGELVGAVITVPAYFDDAQRQATKDAARLAGLNVLRLLNEPTAAAVAYGLDKGAEGLVAIYDLGGGTFDISILRLTRGVFEVLATGGDTALGGDDFDHAIAGWVIEEAGLSADLDPGSQRQLLQIACAAKERLTDEASVRVAYGDWSGELSRATLDELIEPFVARSLKSCRRAVRDSGVDLEEIRSVVMVGGSTRVPRVRTAVGELFGCEPLTDIDPDQVVAIGAAIQADALAGNKRGEELLLLDVIPLSLGLETMGGLMEKVIPRNTTIPVARAQEFTTYKDGQTAMMIHVLQGERELVKDCRSLARFELRGIPPMVAGAAKIRVTFQVDADGLLGVSARELSSGVEASIQVKPSYGLTDGEIARMLKDSFDYAGDDKAARALREQQVEAQRLLEAVQSALDVDGERLLDEEERLAIAAQMDTLRELAGGSDTAAIENQIKRLSQVTDAFAARRMDATVKAALSGRRLNEIEE
Chaperone involved in the maturation of iron-sulfur cluster-containing proteins. Has a low intrinsic ATPase activity which is markedly stimulated by HscB.
B7UWI1
Q73N90
ISPG_TREDE
1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate synthase
Treponema
MNSIKLPRTIHIGGKGQVKKLTLGGTSPILLQTMWKESLLGADLLSIVKSLNELEQLGCDIVRFAVPDMDSAEQFVKLTRLTEMPLVADIHFDYKLALRCMDGDTAKIRINPGNIGSKEKTEEVIRKAKDTGTAIRIGVNSGSLPSDLKKKIEEANSKRNLSGDKKALDDEISLLRADTLTEAAARELEIFEKADFKDAVVSMKASNVRETVMANEIFAKKFDNPLHLGVTEAGPLIQGIVKSTIAFYRLLEQNIGSTIRVSLSDSCENEVIAGREILTECGKRQGGIRLISCPRCGRKGFDVQAFVKRWQTKLLSEKKDISIAVMGCVVNGPGEGKHADLGITGAEDSVIIFKHGAITKRLDLKKLTEEEKIKAVDKAFIEELQSL
Converts 2C-methyl-D-erythritol 2,4-cyclodiphosphate (ME-2,4cPP) into 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate.
Q73N90
B1WUM4
PYRD_CROS5
Dihydroorotate oxidase
Crocosphaera subtropica
MMFNFAQPVYPLVLTAAKNNPENAHQQLLKTLHRLDENRHTVWGKWILENLDHSFTFEDSRLQQNLWGLTFKTPVGLAAGCDKDGLAAGIWDHFGFGFAEIGAVTLHAQPGNPKPRLFRLPQDKAALNRLGANNQGAQKVAQTLKETWQRQPRQIPIGINLCKSKITPLEQAAMDYVGSFRYLEEDADYFVVNVSSPNTPGLRSLQEGEQLNVILQELQSVNSLTKPILVKISPDLSWESIKLIIKLAKTYQLAGIIATNTTIKREGLKTNILEKTGNSIQEEAGGISGQPIRQRSTEVIRFIYEQTQGTLPIIGVGGIFTAEDAWEKITSGASLLQLYTGWIYQGPWCISNINRGLVRKLEKYKLSHISEAVGMDFNS
Catalyzes the conversion of dihydroorotate to orotate with quinone as electron acceptor.
B1WUM4
Q8Z118
SYV_SALTI
Valyl-tRNA synthetase
Salmonella
MEKTYNPQDIEQPLYEHWEKQGYFKPNGDESKESFCIMIPPPNVTGSLHMGHAFQQTIMDTMIRYQRMQGKNTLWQVGTDHAGIATQMVVERKIAAEEGKTRHDYGRDAFIDKIWQWKAESGGTITRQMRRLGNSVDWERERFTMDEGLSNAVKEVFVRLYKEDLIYRGKRLVNWDPKLRTAISDLEVENRESKGSMWHIRYPLADGAKTADGKDYLVVATTRPETVLGDTGVAVNPEDPRYKDLIGKFVILPLVNRRIPIVGDEHADMEKGTGCVKITPAHDFNDYEVGKRHALPMINILTFDGDIRESAEVFDTKGEESNVYSSEIPAEFQKLERFAARKAIVAAVDALGLLEEIKPHDLTVPYGDRGGVVIEPMLTDQWYVRADVLAKPAVEAVENGDIQFVPKQYENMYFSWMRDIQDWCISRQLWWGHRIPAWYDNDGNVYVGRTEDEVRQENNLGADVQLRQDEDVLDTWFSSALWTFSTLGWPENTDALRQFHPTSVMVSGFDIIFFWIARMIMMTMHFIKDENGKPQVPFHTVYMTGLIRDDEGQKMSKSKGNVIDPLDMVDGISLPELLEKRTGNMMQPQMAEKIRKRTEKQFPNGIEPHGTDALRFTLAALASTGRDINWDMKRLEGYRNFCNKLWNASRFVLMNTEEQDCGFNGGEMTLSLADRWILAEFNQTVKAYREALDNFRFDIAAGILYEFTWNQFCDWYLELTKPVMTGGSESELRGTRHTLVTVLEGLLRLAHPIIPFITETIWQRVKVICGITADTIMLQPFPEYNAAQVDEAALADTEWLKQAIVAVRNIRAEMNIAPGKPLELLLRGCSEEAVRRVNDNRSFLLNLARLESITVLPADDKGPVSMTKIIDGAELLIPMAGLINKEDELARLAKEVAKIEGEIARIEGKLSNEGFVARAPEAVIAKEREKLDGYAEAKAKLIEQQAVISAL
Catalyzes the attachment of valine to tRNA(Val). As ValRS can inadvertently accommodate and process structurally similar amino acids such as threonine, to avoid such errors, it has a 'posttransfer' editing activity that hydrolyzes mischarged Thr-tRNA(Val) in a tRNA-dependent manner.
Q8Z118
B3W6P3
MNTH_LACCB
Divalent metal cation transporter MntH
Lacticaseibacillus
MASEDKKSKREHIIHFEDTPSKSLDEVNGSVEVPHNAGFWKTLAAYTGPGILVAVGYMDPGNWITSIAGGASFKYSLLSVILISSLIAMLLQAMAARLGIVTGRDLAQMTRDHTSKAMGGFLWVITELAIMATDIAEIIGSAIALKLLFNMPLIVGIIITTADVLILLLLMRLGFRKIEAVVATLVLVILLVFAYEVILAQPNVPELLKGYLPHADIVTNKSMLYLSLGIVGATVMPHDLFLGSSISQTRKIDRTKHEEVKKAIKFSTIDSNLQLTMAFIVNSLLLILGAALFFGTSSSVGRFVDLFNALSNSQIVGAIASPMLSMLFAVALLASGQSSTITGTLAGQIIMEGFIHLKMPLWAQRLLTRLMSVTPVLIFAIYYHGNEAKIENLLTFSQVFLSIALPFAVIPLVLYTSDKKIMGEFANRAWVKWTAWFISGVLIILNLYLIAQTLGFVK
H(+)-stimulated, divalent metal cation uptake system.
B3W6P3
P23028
PA2HD_PSETE
Acidic phospholipase A2 homolog textilotoxin D chain
Pseudonaja
MHPAHLLVLLGVCVSLLGAASIPRPSLNIMLFGNMIQCTIPCEQSWLGYLDYGCYCGSGSSGIPVDDVDKCCKTHDECYYKAGQIPGCSVQPNEVFNVDYSYECNEGQLTCNESNNECEMAVCNCDRAAAICFARFPYNKNYWSINTEIHCR
Snake venom oligomeric phospholipase A2 that has potent presynaptic neurotoxicity. Chain D is not itself neurotoxic, but it is essential for the neurotoxicity of textilotoxin. Chain D possesses a very low phospholipase activity.
P23028
Q9D0V8
CINP_MOUSE
Cyclin-dependent kinase 2-interacting protein
Mus
MEAKTLGIATPRKPVLSVSARKLKDNAADWHNLILKWDSLSDKGFTTASSIANLKVSLLSKEKVELESSSPASMEEEEKTNLDYDKGLEALCEELQAILDGLTKIQMKMEKLSSTTKGICELENYHYREESSRPPLFHTWPTAFFYEVSRRLSEAYKKELLLKHTIGAELAHTADRNLSLTYLSMWLHQPYIESNSKLQLESMLLETGHRAL
Component of the DNA replication complex, which interacts with two kinases, CDK2 and CDC7, thereby providing a functional and physical link between CDK2 and CDC7 during firing of the origins of replication. Regulates ATR-mediated checkpoint signaling in response to DNA damage. Also involved in the cytoplasmic maturation steps of pre-60S ribosomal particles by promoting the release of shuttling protein RSL24D1/RLP24 from the pre-ribosomal particles. Promotes maturation of pre-60S ribosome together with SPATA5, SPATA5L1 and C1orf109.
Q9D0V8
A9CKB4
4HYPE_AGRFC
4-hydroxyproline 2-epimerase
Agrobacterium tumefaciens complex
MRWKRTLQLLDVHCEGEIGRVVTGGAPKIPGNTVAEQLHWMNTDPQGEALRRFLTLEPRGTPMGSVDLLLPPKHPDAHAAFVILQPDQAHASSGSNSICATTALLESGMVEMQEPETVIILETAAGLVKATATCRDGRCEKVKLTMVPSFVHELDVSIDTPEWGRVTMDISYGGIFYALVDVRQIGLTIEKANAAKLVAAGMTLKDLVNREMTVVHPEIPAISGVAYVMFRDVDADGSIRTCTTMWPGRADRSPCGTGNSANLATLYARGKVKVGDEYKSRSIIGSEFDVGLSAVTEVAGRPAVIPTIAGRGFTFGLHQVGLDPFDPLGDGFAMTDVWGPEAGNI
Catalyzes the epimerization of trans-4-hydroxy-L-proline (t4LHyp) to cis-4-hydroxy-D-proline (c4DHyp). May be involved in a degradation pathway of t4LHyp, which would allow A.tumefaciens to grow on t4LHyp as a sole carbon source. Can also catalyze the epimerization of trans-3-hydroxy-L-proline (t3LHyp) to cis-3-hydroxy-D-proline (c3DHyp) in vitro. Displays no proline racemase activity.
A9CKB4
A3RLD7
CRGB_MACMU
Gamma-B-crystallin
Macaca
MGKITFYEDRAFQGRSYECTTDCPNLQPYFSRCNSIRVESGCWMIYERPNCQGHQYFLRRGEYPNYQQWMGLSDSIRSCHLIPPHSGTYRMKIYERDELRGQMSELTDDCLSVQDRFHLTEIHSLNVLEGSWILYEMPNYRGRQYLLRPGEYRRFLDWGAPNAKVGSLRRVMDLY
Crystallins are the dominant structural components of the vertebrate eye lens.
A3RLD7
A2BQ41
HIS1_PROMS
ATP phosphoribosyltransferase
Prochlorococcus
MITIALPKGALLKDSISTFKKAGLDFSNALEENNRSLTFESNCKRAKALLVRNGDVPVYVSYGQADLGIVGYDVLRESELKVAKLLDLGFGGCHMSLAVKKNSNYLKPTDLPANCKVASKFIKTARSYFEELNIPVEIVHLTGSVELGPITGMAEAIVDLVATGKTLKENGLIKIDDLYYSTARLIGNPLSMRLDDNHLRDTILSIESTNAL
Catalyzes the condensation of ATP and 5-phosphoribose 1-diphosphate to form N'-(5'-phosphoribosyl)-ATP (PR-ATP). Has a crucial role in the pathway because the rate of histidine biosynthesis seems to be controlled primarily by regulation of HisG enzymatic activity.
A2BQ41
Q8EK71
EFG1_SHEON
Elongation factor G 1
Shewanella
MARTTPIERYRNIGICAHVDAGKTTTTERVLFYTGLSHKIGEVHDGAATTDWMVQEQERGITITSAAVTTFWRGMDAQFTEHRINIIDTPGHVDFTIEVERSLRVLDGAVVVFCGASGVEPQSETVWRQADKYRVPRIVFVNKMDRAGADFERVVKQIRTRLGATCVPIQLNIGAEENFTGVIDLIKMKAINWNEADQGMTFSYEAIPAHLTAKAEEMHEFLVEAAAEASDELMDKYLEEGTLSEEEIKKALRQRTINNEIVLATCGSAFKNKGVQAVLDAVVEFLPAPVDVPPIKGIDDNEQEVERPSDDNAPFAALAFKIATDPFVGTLTFIRVYSGVLESGSGVYNSVKQKRERIGRIVQMHANDRTELKEVRAGDIAAAIGLKEVTTGDTLCDNDHKVILERMEFPEPVITIAVEPKSKADQDKMGIALQKLAAEDPSFRVETDEESSQTLISGMGELHLDIIVDRMRREFGVECNVGKPQVAYRETIRGSVEAEGKFVRQSGGRGQFGHVWLKLEPNEEGAGYEFINAIVGGVVPREFIPAVDKGIQEQMKNGVLAGFPVLDVKVTLFDGSYHDVDSNEMAFKIAGSMGFKKGALEAKPVLLEPCMKVEVTTPENYMGDVVGDLNRRRGLIEGMDDGFGGIKIIHAVVPLSEMFGYATDLRSATQGRASYSMEFLKYTDAPQNIAKAIIESRS
Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome.
Q8EK71
Q44906
FLIQ_BORBU
Flagellar biosynthetic protein FliQ
Borreliella
MTAGHILYLIRISIENIIILSAPMLIIALIVGLLISIFQAITSIQDQTLSFIPKIIVILLVIVIFGPWILNKLMQFTYMIFSQLQNV
Role in flagellar biosynthesis.
Q44906
A6T228
HEMH_JANMA
Protoheme ferro-lyase
Janthinobacterium
MSFRTEPPYIHGSTPKTAVVLVNLGTPDAPTTSAVRRYLKQFLSDPRVVEIPRAIWWFILHLVILPFRSGQSAKKYASIWSNEGSPLKVHTEKQAKLLNGYLGERGHKVKVVYAMRYGQPALPDVLRQLKADGCERILFLPAYPQYSGTTTASIFDAVFSHYTQERNVPELRFIKHYHDHDAYIRALRKSVQAHWDMAGRPDKLVMSFHGVPKRTLTLGDPYHCECHKTARLLAKELELTQEQYMVTFQSRFGKAEWLQPYTAPTLQKLAKEGIGRVDVICPGFTSDCLETLEEIAMEARHDFMSAGGKDFNYIGCLNEDDAWIKAMAEITELHLIGWPTIVPPSLREEQEQQAHISREEARRLGADQ
Catalyzes the ferrous insertion into protoporphyrin IX.
A6T228
Q9JX02
RL11_NEIMA
50S ribosomal protein L11
Neisseria
MAKKIIGYIKLQIPAGKANPSPPVGPALGQRGLNIMEFCKAFNAATQGMEPGLPIPVVITAFADKSFTFVMKTPPASILLKKAAGLQKGSSNPLTNKVGKLTRAQLEEIAKTKEPDLTAADLDAAVRTIAGSARSMGLDVEGVV
Forms part of the ribosomal stalk which helps the ribosome interact with GTP-bound translation factors.
Q9JX02
Q70RW3
CYB_HYPAP
Ubiquinol-cytochrome-c reductase complex cytochrome b subunit
Hyperoodon
MINIRKTHPLMKIINNTFIDLPTPSNISSWWNFGSLLGLCLITQILTGLFLAMHYTPDTTTAFSSIAHICRDVNYGWVIRYLHANGASMFFICLYAHIGRGLYYGSYIFLETWNIGVILLFTVMATAFMGYVLPWGQMSFWGATVITNLLSAIPYIGTTLVEWIWGGFSVDKATLTRFFALHFILPFIILALAIVHLLFLHETGSNNPTGIPSDMDKIPFHPYYTIKDTLGALLLILVLLTLTLFAPDLLGDPDNYTPANPLSTPAHIKPEWYFLFAYAILRSIPNKLGGVLALLLSILILLFIPLLHTSKQRSMMFRPFSQLLFWLLIADFLTLTWIGGQPVEHPYMIMGQLASMLYFLLILVLMPMASLIENKLLKW
Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex) that is part of the mitochondrial respiratory chain. The b-c1 complex mediates electron transfer from ubiquinol to cytochrome c. Contributes to the generation of a proton gradient across the mitochondrial membrane that is then used for ATP synthesis.
Q70RW3
B6JP93
TSAD_HELP2
tRNA threonylcarbamoyladenosine biosynthesis protein TsaD
Helicobacter
MILSIESSCDDSSLALTRIKDAQLIAHFKISQEKHHSSYGGVVPELASRLHAENLPLLLERIKISLNKDFSKIKAIAITNQPGLSVTLIEGLMMAKALSLSLNLPLILEDHLRGHVYSLFINEKQTCMPLSVLLVSGGHSLILEARDYENIKIVATSLDDSFGESFDKVSKMLDLGYPGGPIVEKLALDYRHPNEPLMFPVPLKNSPNLAFSFSGLKNAVRLEVEKNAPNLNDEVKQKIGYHFQSAAIEHLIQQTKRYFKTKRPKIFGIVGGASQNLALRKAFENLCDAFDCKLVLAPLEFCSDNAAMIGRSSLEAYQKKRFVPLEKANISPRTLLKSFE
Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. Is involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37, together with TsaE and TsaB. TsaD likely plays a direct catalytic role in this reaction.
B6JP93
Q8CTP4
LARC_STAES
Nickel-pincer cofactor biosynthesis protein LarC
Staphylococcus
MTKALYLDCHAGIAGDMLLSALVDLGANPEDIESELKKLPLDQFKLHFQKRVKQGIHAMTLNIDVKEANHHRHVNDIFKMIDDSTLPERVKYRSKKIFEIIGQAEAKIHGMSFEEVHFHEVGAMDSIIDIIGGCIALEQLGINTLYCSAIPTGHGKINIAHGIYPIPAPATAEILKGIPIAHFDVQSELTTPTGAAFAKGLVSSFGPFPSATIQHIGYGAGSKDFDFPNILRVIQFESEFEQQDSVQVIECQIDDMTPEALGYFMNNALEQGALDAYYTPIFMKKSRPSTQLTLICKLHDKTYFEQLILQETSSLGVRSTSVNRKTLNRAFKILSTQHGTVSIKFGLQNGKIMKMKPEYEDLKKIAKTTKQPFQVIHNEVLQQLYQTYHIGNILQ
Involved in the biosynthesis of a nickel-pincer cofactor ((SCS)Ni(II) pincer complex). Binds Ni(2+), and functions in nickel delivery to pyridinium-3,5-bisthiocarboxylic acid mononucleotide (P2TMN), to form the mature cofactor. Is thus probably required for the activation of nickel-pincer cofactor-dependent enzymes.
Q8CTP4
Q5FQB4
GLMM_GLUOX
Phosphoglucosamine mutase
Gluconobacter
MATKRSLFGTDGIRGTANTAPMTVEIAQRLGQAAGLYFMRSQNRRHSVVLGKDTRLSGYMLECALVAGFLSAGMDVILVGPLPTPAIAMLTRSLRADLGVMVSASHNPFTDNGIKLFGPDGFKLSDEVEGEIEDLMSQDLSARLASPAQIGRASRLTDAAGRYIENAKASFPRGLRLDGLKIVIDCANGSAYRVAPTALWELGAEVIKIGCSPDGLNINDGVGSTHPETLCAAVREHGADFGIALDGDADRVLIADENGNLVDGDQIIGLIAAFWKQHDRLRGNTVVTTVMSNMGLEKALAENGLELQRTAVGDRYVVERMREIGANLGGEQSGHMVLSDYATTGDGLIAALQVLAVSVETKRPASEICRFFTPYPQLLKNVRYSGTSPMSSPDLAAAKAWADERLAGSGRLVLRASGTEPLIRVMAEAQDEALVHEVVDHVCDVIRAIAHA
Catalyzes the conversion of glucosamine-6-phosphate to glucosamine-1-phosphate.
Q5FQB4
A7VN14
MSMB2_PROFL
Small serum protein 2
Protobothrops
MRVFFSLIIFSFMLATCQGACGIGPLVSSPTDAMAPKKCVDPNDRRKHLIVSTWNTADCLRCECDNDGLSCCHRYGGLAERAGCKSVLNQVTCEYEFYRLDDLSKRCDA
May serve as a self-defense protein against the toxic effects of the snake venom during accidental envenomation. Does not show inhibitory activity towards brevilysin H6.
A7VN14
Q5YYB6
IDI_NOCFA
Isopentenyl pyrophosphate isomerase
Nocardia
MPVELVDEAGRAVGACPVAEAHRDPGKLHRAFSVLLFDTAGRVLLQQRAAVKTRFPLLWANTCCGHPAPGESVEAAAATRLAEELGVAAGLTEVGVFRYRAADTATGRVEHEWDHVLIGTLDTTPHPDPAEVANLRWVRPAEVRAKLAAEPAAYTPWLAEVLEIADAAYRESAGR
Catalyzes the 1,3-allylic rearrangement of the homoallylic substrate isopentenyl (IPP) to its highly electrophilic allylic isomer, dimethylallyl diphosphate (DMAPP).
Q5YYB6
Q41005
CBPX_PEA
Serine carboxypeptidase-like
Pisum
TGESYAGHYIPALASRIHQGNQANEGIHINLKGLAIGNGLTNPAIQYKGYPDYALDMGIITQTTHDLLGKVLVPACELAIKLCGTNGKVSCLTANVACNLIFSDIMLHAGGVNYYDIRKKCEGSLCYDFSNMEKFLNQESVRDSLGVGKIRFVSCSTEVYMAMLVDWMRNLEVGIPLLLEDGINLLIYAGEYDLICNWLGNSRWVHAMKWSGQKEFVASSDVPFVVNGSQAGLLKSYGPLSFLKVHDAGHMVPMDQPKAALEMVKQWTRGTLAESIDGEEKLVADM
Involved in degradation of small peptides.
Q41005
Q8Z9A6
DXR_SALTI
2-C-methyl-D-erythritol 4-phosphate synthase
Salmonella
MKQLTILGSTGSIGCSTLDVVHHNPDSFRVIALVAGKNVARMAEQCLEFSPRYAVMDDTSSAEQLKIMLQQHGSRTEVLSGQQAACEMAALDEVGHVMAAIVGAAGLLPTLAAIRAGKTILLANKESLVTCGRLFMDEVKRSNARLLPVDSEHNAIFQSLPQSIQHNLGYADLEQNGVTSILLTGSGGPFRETPMCDLAAMTPDQACRHPNWSMGRKISVDSATMMNKGLEYIEARWLFNASARQMEVLIHPQSVIHSMVRYQDGSVLAQLGEPDMRTPIAHTMAWPNRVTSGAQPLDFCKLSALTFSAPDYQRYPCLKLAMEAFEQGQAATTALNAANEITVAAFLAQQIRFTDIAGLNLAVLERMDLHEPASVDDVLQVDAIAREVARKQVIRLSR
Catalyzes the NADPH-dependent rearrangement and reduction of 1-deoxy-D-xylulose-5-phosphate (DXP) to 2-C-methyl-D-erythritol 4-phosphate (MEP).
Q8Z9A6
A4XXN9
RSMJ_PSEMY
rRNA (guanine-N(2)-)-methyltransferase
Pseudomonas
MTDEPRNASIRMDALQAHHAEAAARWATRLGLPRVGETDFALQLGDQGLQLVELGDKAPGPVRVDFVEGAAAHRRQFGGGSGQMIAKAVGVQSGIRPRILDATAGLGRDAFVLASLGCEMTLIERQPLIAALLEDGLQRAELDLEVAPIAARMRLLTGNAIDLMQNWQGEAPQVIYLDPMFPHRDKSALVKKEMRLFRPFVGDDLDAPALLAAALALASHRVVVKRPRKAPAIEGTKPGYVLEGKSSRYDVYPKKKLEGA
Specifically methylates the guanosine in position 1516 of 16S rRNA.
A4XXN9
A4XL26
HIS1_CALS8
ATP phosphoribosyltransferase
Caldicellulosiruptor
MVTIALPKGRLTEEATELFQRSSLISIDISQETRKLVLEDPRGNLRFLMVKPFDVPTYVEYGIADMGIVGKDVLLEVNKKVYELLDLKIGKCFIALAGPKGLREELLKKPEKIIATKFPNITKEYFENVLGEDVQIIKLNGSVELAPILGLSDMIVDIVESGRTLRENGLEVYEKLYDISARLIINRASLKLKREIEGIVNCLERMILQ
Catalyzes the condensation of ATP and 5-phosphoribose 1-diphosphate to form N'-(5'-phosphoribosyl)-ATP (PR-ATP). Has a crucial role in the pathway because the rate of histidine biosynthesis seems to be controlled primarily by regulation of HisG enzymatic activity.
A4XL26
A5DG70
GUF1_PICGU
Ribosomal back-translocase
Meyerozyma
MYIHSSRTVLARYGSRTPLLRPSVLGRYSTSPAATIEARKIALNRDNYIKSVYDRIAKIPPENYRNFSIVAHVDHGKSTLSDRLLELTGVIQPGDKNQVLDRLDVERERGITVKAQTCTMIFNDPRNGQDYLLHLVDTPGHVDFRAEVSRSYASCGGALLLVDATQGVQAQTVANFYLAYSMGLKLIPIINKIDLDAADIPRAMDQVESTFELDRENCLQVSAKTGLNVKSILPAIVDHIPAPDCDINSPLKALLVDSWHDPYVGVVMLLYVKEGTIKKGMKLLSAHTEGRYEVKEVGIMYPDKVPMESIRAGQVGYIVPGMKDPSQAKIGDTFFQYGKHEGLEALPGFEEPKPMVFVGAFPAEGSEFKVMDDHIANLVLNDRSVTLEKETSNALGLGWRLGFLGSLHASVFQERLENEYGAKIILTAPTVPYKIVYKDGTDKIVTNPDEFPGSDLRNQNVDKLMEPYVNAIMTIPDEYIGAVMSLCENNRGIQKELEYLTNGQVLMRYEIPLAQLVEDFFGKLKGCTKGYASLDYEDAGYKKSDIVKMELCVNGEPQDALTQVMHRSQVQARGKEYVVRFKEYLRFQLFEVAIQAKVNNKVVARETIKAKRKDVTQKLHAADISRRKKLLSRQKEGKKQMKASGRVHINHEAYQAFLRRTI
Promotes mitochondrial protein synthesis. May act as a fidelity factor of the translation reaction, by catalyzing a one-codon backward translocation of tRNAs on improperly translocated ribosomes. Binds to mitochondrial ribosomes in a GTP-dependent manner.
A5DG70
A1JTD7
RSMG_YERE8
16S rRNA 7-methylguanosine methyltransferase
Yersinia
MLKKLDSLLSAAGIELPDQQKHQLIGYVELLDKWNKAYNLTSVRDPMQMLVRHILDSIVVNPHLQGSRFIDVGTGPGLPGIPLAIVRPDAHFVLLDSLGKRVRFLRQVQHELGLSNIEPVQSRVEDFAAKPPFDGVISRAFASLQDMLSWCHHLPAKPEGRFYALKGVRPDDELATLPEGIVVESVVRLRVPELDGERHLVILKSN
Specifically methylates the N7 position of guanine in position 527 of 16S rRNA.
A1JTD7
Q1REM0
KDPB_ECOUT
Potassium-translocating ATPase B chain
Escherichia
MSRKQLALFEPTLVVQALKEAVKKLNPQAQWRNPVMFIVWIGSLLTTCISIAMASDVMPGNALFSAAISGWLWVTVLFANFAEALAEGRSKAQANSLKGVKKTAFARKLREPKYGAAADKVPADQLRKGDIVLVEASDIIPCDGEVIEGGASVDESAITGESAPVIRESGGDFASVTGGTRILSDWLVIECSVNPGETFLDRMIAMVEGAQRRKTPNEIALTILLIALTIVFLLATATLWPFSAWGGNAVSVTVLVALLVCLIPTTIGGLLSAIGVAGMSRMLGANVIATSGRAVEAAGDVDVLLLDKTGTITLGNRQASEFIPAQGVEEKALADAAQLASLADETPEGRSIVILAKQRFNLRERDVQSLHATFVPFTAQSRMSGINIDNRMIRKGSVDAIRRHVEANGGHFPADVDQKVDQVARQGATPLVVVEGSRVLGVIALKDIVKGGIKERFAQLRKMGIKTVMITGDNRLTAAAIAAEAGVDDFLAEATPEAKLALIRQYQAEGRLVAMTGDGTNDAPALAQADVAVAMNSGTQAAKEAGNMVDLDSNPTKLIEVVHIGKQMLMTRGSLTTFSIANDVAKYFAIIPAAFAATYPQLNALNIMRLHSPDSAILSAVIFNALIIVFLIPLALKGVSYKPLTASAMLRRNLWIYGLGGLLVPFIGIKVIDLLLTVCGLV
Part of the high-affinity ATP-driven potassium transport (or Kdp) system, which catalyzes the hydrolysis of ATP coupled with the electrogenic transport of potassium into the cytoplasm. This subunit is responsible for energy coupling to the transport system and for the release of the potassium ions to the cytoplasm.
Q1REM0
Q82QN1
Y474_STRAW
Putative S-adenosyl-L-methionine-dependent methyltransferase SAV_474/SAV474
Streptomyces
MTDEQERVQPSGVWATAVGVARVRALETERENALFRDPLAQAFATAGGLWPSSPPLPDDEAARRRRLTVSFSIVIRTKFLDDLLQQASASGVRQVVLLGAGMDSRAFRMDWPEGTRLFEVDTAAPLDFKASVLRQERADARCERITVAVDLREDWPGALAAVGHDPAVPTVWIAEGLLIYLPEDAVELLLARISAQSAAGSRMGLTLGSRGVIERFGADAAPGSAASMWVSEMPDDPVGWLAGHGWEADSHTLRERAAAYGRPISTPPQREERPGGLISAVRR
Exhibits S-adenosyl-L-methionine-dependent methyltransferase activity.
Q82QN1
Q99ZD0
PFKA_STRP1
Phosphohexokinase
Streptococcus
MKRIAVLTSGGDAPGMNAAIRAVVRKAISEGMEVYGINRGYAGMVDGDIFPLGSKEVGDKISRGGTFLYSARYPEFAQLEGQLAGIEQLKKHGIEGVVVIGGDGSYHGAMRLTEHGFPAVGIPGTIDNDIAGTDYTIGFDTAVNTAVEAIDKLRDTSSSHGRTFVVEVMGRNAGDIALWAGIASGADQIIVPEEEFDIEKVASTIQYDFEHKGKNHHIIVLAEGVMSGEAFAQKLKEAGDKSDLRVTNLGHILRGGSPTARDRVIASWMGSHAVELLKDGKGGLAVGIHNEELVESPILGTAEEGALFSLTEEGKIIVNNPHKARLDFAALNRSLSQ
Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis.
Q99ZD0
P25672
3L24_NAJNA
Toxin D
Naja
IRCFITPDITSKDCPNGHVCYTKTWCDGFCRIRGERVDLGCAATCPTVKTGVDIQCCSTDDCDPFPTRKRP
Binds with high affinity to muscular (alpha-1/CHRNA1) and neuronal (alpha-7/CHRNA7) nicotinic acetylcholine receptor (nAChR) and inhibits acetylcholine from binding to the receptor, thereby impairing neuromuscular and neuronal transmission.
P25672
P68046
HBB_ODORO
Hemoglobin beta chain
Odobenus
VHLTADEKAAVTALWGKVNVDEVGGEALGRLLVVYPWTQRFFDSFGDLSSPDAVMGNPKVKAHGKKVLNSFSDGLKNLDNLKGTFAKLSELHCDKLHVDPENFKLLGNVLVCVLAHHFGKEFTPQVQAAYQKVVAGVANALAHKYH
Involved in oxygen transport from the lung to the various peripheral tissues.
P68046
Q5R530
NXPH1_PONAB
Neurexophilin-1
Pongo
MQAACWYVLLLLQPTIYLVTCANLTNGGKSELLKSGSSKSTLKHIWTESSKDLSISRLLSQTFRGKENDTDLDLRYDTPEPYSEQDLWDWLRNSTDLQEPRPRAKRRPIVKTGKFKKMFGWGDFHSNIKTVKLNLLITGKIVDHGNGTFSVYFRHNSTGQGNVSVSLVPPTKIVEFDLAQQTVIDAKDSKSFNCRIEYEKVDKATKNTLCNYDPSKTCYQEQTQSHVSWLCSKPFKVICIYISFYSTDYKLVQKVCPDYNYHSDTPYFPSG
May be signaling molecules that resemble neuropeptides and that act by binding to alpha-neurexins and possibly other receptors.
Q5R530
P75250
IPYR_MYCPN
Pyrophosphate phospho-hydrolase
Mycoplasma
MDKFLIDVTVEIPKSSKIKYEYDRKTSQIRVDRILFGSESYPQNYGFIANTLDWDGDELDCFIFADQAFLPGVVVPTRIVGALEMVDDGELDTKLLGVIDCDPRYKEINSVNDLPKHRVDEIIGFLKTYKLLQKKEVIIKGVQSLEWAKKEYQVCVDLMKQYGKLPKDEFIAKMQKLHPEHYQK
Catalyzes the hydrolysis of inorganic pyrophosphate (PPi) forming two phosphate ions.
P75250
Q9TDK2
CYB_DELCT
Ubiquinol-cytochrome-c reductase complex cytochrome b subunit
Delphinus
MTNIRKTHPLMKILNDAFIDLPTPSNISSWWNFGSLLGLCLIMQILTGLFLAMHYTPDTSTAFSSVAHICRDVNYGWFIRYLHANGASMFFICLYAHIGRGLYYGSYMFQETWNIGVLLLLTVMATAFVGYVLPWGQMSFWGATVITNLLSAIPYIGTTLVEWIWGGFSVDKATLTRFFAFHFILPFIITALAAVHLLFLHETGSNNPTGIPSNMDMIPFHPYYTIKDILGALLLILTLLALTLFTPDLLGDPDNYTPANPLSTPAHIKPEWYFLFAYAILRSIPNKLGGVLALLLSILILIFIPMLQTSKQRSMMFRPFSQLLFWTLVADLLTLTWIGGQPVEHPYIIVGQLASILYFLLILVLMPTAGLIENKLLKW
Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex) that is part of the mitochondrial respiratory chain. The b-c1 complex mediates electron transfer from ubiquinol to cytochrome c. Contributes to the generation of a proton gradient across the mitochondrial membrane that is then used for ATP synthesis.
Q9TDK2
Q2RJM0
RS15_MOOTA
30S ribosomal protein S15
Moorella
MALDAAKKREIIARYQKHENDTGSPEVQIAILTERINHLTEHLQVHHKDHHSRRGLLKMVGQRRGLLNYLRENDVERYRQIVESLGLRR
Forms an intersubunit bridge (bridge B4) with the 23S rRNA of the 50S subunit in the ribosome.
Q2RJM0
A7ZHS1
LPXA_ECO24
Acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase
Escherichia
MIDKSAFVHPTAIVEEGASIGANAHIGPFCIVGPHVEIGEGTVLKSHVVVNGHTKIGRDNEIYQFASIGEVNQDLKYAGEPTRVEIGDRNRIRESVTIHRGTVQGGGLTKVGSDNLLMINAHIAHDCTVGNRCILANNATLAGHVSVDDFAIIGGMTAVHQFCIIGAHVMVGGCSGVAQDVPPYVIAQGNHATPFGVNIEGLKRRGFSREAITAIRNAYKLIYRSGKTLDEVKPEIAELAETYPEVKAFTDFFARSTRGLIR
Involved in the biosynthesis of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell.
A7ZHS1
Q6FZS8
GATC_BARQU
Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit C
Bartonella
MSVDQETVKRVSHLARIAIHDDEIEPMTKELNVILGFVEQLNEVDVNGIEPLTSVMPMALRMREDSVTDGDKVADIVANAPVTEENFFLVSKVVE
Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl-tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an activated phospho-Asp-tRNA(Asn) or phospho-Glu-tRNA(Gln).
Q6FZS8
Q07V68
MIAB_RHOP5
tRNA-i(6)A37 methylthiotransferase
Rhodopseudomonas
MDQPRKLHIKSFGCQMNVYDAQRMVDALAPEGFVETQSADDADLVILNTCHIREKAAEKVYSELGKLRLLKQDAASHGRRFEIAVAGCVAQAEGAEIIRRQPAVDVVVGPQSYHHLPELLEKARRDGRALETEFPIEDKFGVLPPPRPDAIRARGVSAFVTVQEGCDKFCSFCVVPYTRGAEMSRPVAKILDDVKRLIDNGVREITLIGQNVNAYHGEGPDDRPWTLGALLRHLASVPGVARLRYSTSHPLDVDDELIAAHRELPGLMPFVHLPVQSGSDAILAAMNRRHSADDYRRVIDRFRQADPSIAFSSDFIVGFPGETDRDFEATLALVTQIGYAGAYSFKYSPRPGTPAAELQEMVAPAVMDQRLEQLQGLIDSQQAAFNRASIGTTVDVLFERAARHPGQIVGRTAYLQPAHVMAADDIVGQVLPVTIHSLERYSLIGELVKPQPARPPKPLPVTTGA
Catalyzes the methylthiolation of N6-(dimethylallyl)adenosine (i(6)A), leading to the formation of 2-methylthio-N6-(dimethylallyl)adenosine (ms(2)i(6)A) at position 37 in tRNAs that read codons beginning with uridine.
Q07V68
Q03745
CR1EB_BACTA
Insecticidal delta-endotoxin CryIE(b)
Bacillus cereus group
MENNIENQCIPYNCLNNPEVEILGIERSNSNVAAEIGLGLSRLLVSRIPLGDFILGLFDVIWGAIGPSQWDIFLEQIELLIGQRIEEFARNQAISRLQGLSNLYRIYTNAFKNWEVDPTNPALREEMRIQFNDMNSALTTAIPLFSVQGYEIPLLSVYVQAANLHLSVLRDVSVFGQRWGFDVATINSRYNDLTRLIGEYTDYAVRWYNTGLNRLPRNEGVRGWARFNRFRRELTISVLDIISFFQNYDSRLYPIPTIYQLTREVYTDPVINITDYRVTPSFESIENSAIRSPHLMDFLNNIIIDTDLIRGVHYWAGHRVTSHFTGSSQVISSPQYGITANAEPSRTIAPSTFPGLNLFYRTLSDPFFRRSDNIMPTLGINVVQGVGFIQPNNGEVLYRRRGTVDSLDELPIDGENSLVGYSHRLSHVTLTRSLYNTNITSLPTFVWTHHSATDRNIIYPDVITQIPLVKSFSLTSGTSVVRGPGFTGGDIIRTNVNGNVLSMSLNFSNTSLQRYRVRVRYAASQTMVMRVNVGGSTTFDQGFPSTMSANGSLTSQSFRFAEFPVGISTSGSQTAGISISNNPGRQTFHLDRIEFIPVDATFEAEYDLERAQKAVNSLFTSSNQIELKTDVTDYHIDQVSNLVDCLSDEFCLDEKRELSEKVKHAKRLSDERNLLQDPNFRGINRQPDRGWRGSTDITIQGGDDVFKENYVTLPGTFDECYPTYLYQKIDESKLKAYNRYQLRGYIEDSQDLEIYLIRYNAKHETVNVPGTGSLWPLSVESPIGRCGEPNRCVPHLEWNPDLDCSCRDGEKCAHHSHHFSLDIDVGCTDLQEDLGVWVVFKIKTQEGYARLGNLEFIEEKPLIGEALSRVKRAEKKWRDKREKLQLETKRVYTEAKEAVDALFVDSQYDRLQADTNIGMIHAADRLVHQIHEAYLPELPFIPGINVVIFEELENRISTALSLYDARNVIKNGDFNNGLSCWNVKGHVDVVEQNNHRSVLVVPEWEAEVSQTIRVCPGRGYILRVTAYKEGYGEGCVTIHEIENNTDELKFKNCEEEEVYPTDTGTCNDYTAHQGTAGSTDSCNSRNIRYEDAYEMNTTASVNYKPTYEEERYTDVQGDNHCEYDRGYVNYRPVPAGYVTKELEYFPETDKVWIEIGETEGKFIVDNVELLLMEE
Promotes colloidosmotic lysis by binding to the midgut epithelial cells of many lepidopteran larvae.
Q03745
A9I7J3
CCME_BORPD
Heme chaperone CcmE
Bordetella
MTPQRKRRLVMLAALAGGVGVAVALALAALQQNINLFYSPSQIAAGEAPLHTRIRAGGLVQDGSLRRAPDSLAVQFGITDGVQQVLVRYDGILPDLFREGQGIVALGKLDAQGMLQADEVLAKHDQNYMPPEAAHALKQGAATSGGTPAAEPQP
Heme chaperone required for the biogenesis of c-type cytochromes. Transiently binds heme delivered by CcmC and transfers the heme to apo-cytochromes in a process facilitated by CcmF and CcmH.
A9I7J3
B3PVT4
AROE_RHIE6
Shikimate dehydrogenase (NADP(+))
Rhizobium
MGDSRETFGPKAFVTGFPIKHSRSPLIHGYWLKTLGLPGSYRAHEVAPEAFADFIASLKDGSSGFAGGNVTIPHKELAFRLADRPDALSQELGASNTLWLEDDLLHATNTDGRGFTANLDERHPGWDRHDTAVIFGAGGASRAIIQAVRDRGFKTIHVVNRTVGRARELADRFGPKVHAHPAGALAEVMKGAGLFINTTSLGMDGEAAPQLDFTPLTADAVVTDIVYVPLKTPLLAQAQEQGFPIVDGLGMLLHQAVPGFEKWFGKRPVVDAALRALIIADMEAH
Involved in the biosynthesis of the chorismate, which leads to the biosynthesis of aromatic amino acids. Catalyzes the reversible NADPH linked reduction of 3-dehydroshikimate (DHSA) to yield shikimate (SA).
B3PVT4
Q8XXF5
RNPH_RALSO
tRNA nucleotidyltransferase
Ralstonia
MRPSGRQPDQLRPVTLTRHYTRHAEGSVLVCFGDTHVLCTASVLPKVPPHKKGSGEGWVTAEYGMLPRSTHTRSDREAARGKQSGRTQEIQRLIGRAMRSVFDLSALGEHTIHLDCDVLQADGGTRTASITGAFVAAHDAISVMRKKGQLTGEPIRDFVAAVSVGVVDGVPVLDLDYPEDASCDTDMNIVMTGAGGFVEVQGTAEGTPFTRTEMDALLGLADHGIRTLIGLQKQALGL
Phosphorolytic 3'-5' exoribonuclease that plays an important role in tRNA 3'-end maturation. Removes nucleotide residues following the 3'-CCA terminus of tRNAs; can also add nucleotides to the ends of RNA molecules by using nucleoside diphosphates as substrates, but this may not be physiologically important. Probably plays a role in initiation of 16S rRNA degradation (leading to ribosome degradation) during starvation.
Q8XXF5
Q47AZ9
UBIC_DECAR
Probable chorismate pyruvate-lyase
Dechloromonas
MKRSKWRTRFAGAYCDPILRSWLTEPDSLTARCQRASSAFRVRLLRYGKGQALADEAVEGKAGRHSAWVREVVLECDGVPVIFAHTTLSTARRGRMTRWMAGLGSRSLGSLLFAYPGFKRGGIEFLRLDRCHPLYRRAAALGAGRKSLWARRSLHRLGGQQVLVTEVFLPAITLLK
Removes the pyruvyl group from chorismate, with concomitant aromatization of the ring, to provide 4-hydroxybenzoate (4HB) for the ubiquinone pathway.
Q47AZ9
Q6FKS8
SPB4_CANGA
ATP-dependent rRNA helicase SPB4
Nakaseomyces/Candida clade
MGKSLEWADLDYELQPWIKKAINVSGFDSMTPVQASTIPMFAKNKDVVVESVTGSGKTIAFVIPILEKIISEGINNSKFKKGHFYSLILAPTRELSMQIQNVVSSFLEHYPEDQYPIRSQLVVGTNEKSVRDDVNTLLDERPQILIGTPGRVLDFLQSPSVKTSSCGMVVLDEADRLLDVSFFKDVEKILNVLPKQRRTGLFSATISSAGTLIFKTGLRNPVKITVNSQGKNAPTTLNLFYSVMKPEEKLQNLIHIMNNIRFKKCIVYFSTCVSVTFFYQYLKYLQQTDKTLREDLQVISIHGKLTTQSRRKALSTFTESLSDCILLTTDVAARGIDIPDVDLVLQIDPPTDADIFLHRCGRTGRANKIGRAIVFLNEGREEDYIPFMEVKNVDIEETDINKNKISNDNNDEFYQRFTKWLLSDRANYDLSVKSYVAFIRYYSKHSATSIFRLQSLDYVSLGKMYGLFRLPRMPEITKYLQDKEKSGETVVGYYGEGWLMNPPPIDMDKYAYQDKKREKARIEELKNLAQINDKKKLKAELKKKNMAWSSKTMTKEERQERRKKLDLKRKAIELEIAAEAERDESDTEITQDWKDEILQKKKKKKVGSEMQGSFDDL
ATP-binding RNA helicase involved in the biogenesis of 60S ribosomal subunits. Binds 90S pre-ribosomal particles and dissociates from pre-60S ribosomal particles after processing of 27SB pre-rRNA. Required for the normal formation of 18S rRNA through the processing of pre-rRNAs at sites A0, A1 and A2, and the normal formation of 25S and 5.8S rRNAs through the processing of pre-rRNAs at sites C1 and C2.
Q6FKS8
P24823
PPBN_MOUSE
Embryonic-type alkaline phosphatase
Mus
MWGACLLLLGLSLQVCPSVIPVEEENPAFWNRKAAEALDAAKKLKPIQTSAKNLVILMGDGMGVSTVTATRILKGQQQGHLGPETQLAMDRFPHMALSKTYNTDKQIPDSAGTGTAFLCGVKTNMKVIGLSAAARFNQCNTTWGNEVVSVMHRAKKAGKSVGVVTTTSVQHASPAGTYAHTVNRGWYSDAQMPASALQDGCKDISTQLISNMDIDVILGGGRKFMFPKGTPDQEYPTDTKQAGTRLDGRNLVQEWLAKHQGARYVWNRSELIQASLNRSVTHLMGLFEPNDMKYEIHRDPAQDPSLAEMTEVAVRMLSRNPKGFYLFVEGGRIDHGHHETVAYRALTEAVMFDSAVDKADKLTSEQDTMILVTADHSHVFSFGGYTQRGASIFGLAPFKAEDGKSFTSILYGNGPGYKLHNGARADVTEEESSNPTYQQQAAVPLSSETHSGEDVAIFARGPQAHLVHGVQEQNYIAHVMAFAACLEPYTDCGLASPAGQSSAVSPGYMSTLLCLLAGKMLMLMAAAEP
Alkaline phosphatase that can hydrolyze various phosphate compounds.
P24823
A6W572
UPP_KINRD
UPRTase
Kineococcus
MRLSVIDHPLVAHKLTALRDARTDSPTFRRLADELVTLLAYEATRDVAVEPHPVTTPVTATTGVRLTSPKPIVVPILRAGLGMLDGMVRLLPTAEVGFLGMIRDETTLQATTYANRLPDDLSGRQVFVLDPMLATGGTLVAAITYLLERGARDVTALCLLAAPEGLEVVRTAFDDHAQVTVVTAAVDERLDENGYIVPGLGDAGDRLYGVV
Catalyzes the conversion of uracil and 5-phospho-alpha-D-ribose 1-diphosphate (PRPP) to UMP and diphosphate.
A6W572
O94229
IDH1_KLULA
NAD(+)-specific ICDH
Kluyveromyces
MLRQGIAAQKKSFATLAAEQLLPKKYGGRYTVTLIPGDGVGKEVTDSVVKIFENENIPIDWETIDISGLENTENVQRAVESLKRNKVGLKGIWHTPADQTGHGSLNVALRKQLDIFANVALFKSIPGVKTRLNNIDMVIIRENTEGEYSGLEHESVPGVVESLKIMTRAKSERIARFAFDFALKNNRKSVCAVHKANIMKLGDGLFRNTVNEIGANEYPELDVKNIIVDNASMQAVAKPHQFDVLVTPNLYGSILGNIGSALIGGPGLVPGANFGREYAVFEPGSRHVGLDIKGQNVANPTAMILSSTLMLRHLGLNAYADRISKATYDVISEGKSTTRDIGGSASTSEFTNAVIEKLAKL
Performs an essential role in the oxidative function of the citric acid cycle.
O94229
Q2P472
DXS_XANOM
1-deoxyxylulose-5-phosphate synthase
Xanthomonas
MIDTTRYPRLSRIHTPDDLRRFDEAELTVIAEELRSYLIESVGKSGGHFAAGLGVIELTVALHYLYQTPVDQLVWDVGHQTYPHKILTGRRDQIHTVKQKDGVAPFPKREESVYDTFGVGHSSTSISAALGMAIAAQRNGDDRKVVAVIGDGAMTAGMVYEALNHAGGMDPEPNLLVILNDNRMSISEAVGGLTKMLGRASGSRTLNAIREGGKKILGDKKNNPTARFVRRWEEHWKGMFVPSTLFEEMGFHYTGPIDGHDLPRLVGALKTLQTLKGPQLLHVITTKGKGYELAEGDQIGYHAVSPFDPSKGLVAKGGAKKPTYTDVFSDWVCDMAAAEPKLLVITPAMREGSGLVRFSKEYPQRYFDVAIAEQHAVTLAAGMATQGAKPVVAIYSTFLQRGYDQLVHDVAVQQLDVLFAIDRGGVVGPDGATHAGNLDLSFLRCVPHMVVMAPADEAECRQMLSTGMQYQGPAAVRYPRGTGPGAALDSSLATLPIGKAQLRHSGTRIALLGFGATVDAAEAVGRDLGLTVVNMRFVKPLDKAMLLELAKTHEGFVTIEDNVVAGGAGSGVSELLNAEAITLPMLHLGLPDSFQHHASREDLLAEAGIDQAGIRTAVLKRWPQLMTGKTPSLNAAAG
Catalyzes the acyloin condensation reaction between C atoms 2 and 3 of pyruvate and glyceraldehyde 3-phosphate to yield 1-deoxy-D-xylulose-5-phosphate (DXP).
Q2P472
P45110
ARGR_HAEIN
Arginine repressor
Haemophilus
MTENLTRAFKELLNQERFGSQSEIVDALKKQGFTGINQSKISRMLSKFGAVRTRNTKMEMVYCLPNELSVPNTSSPLKNLVLDVDHNAMLIVIKTTPGAAQLIARLLDSIGKSEGILGTIAGDDTIFVTPTNNKPIDELLQNIQRLFENTL
Regulates arginine biosynthesis genes.
P45110
P40684
DCUA_SERMA
C4-dicarboxylate transporter DcuA
Serratia
MLAVELVIVLLAIFLGARLGGIGIGFAGGLGVLALALIGVKPGNIPFDVISIIMAVIAAISAMQVAGGMDYLVQQTEKLLRKNPKHITILAPIVTYFLTIFAGTGNISLSALPVIAEVAKEQGIKPCRPLST
Responsible for the transport of C4-dicarboxylates during aerobic and anaerobic growth. Required for the uptake of L-aspartate as a nitrogen source during aerobic growth. The uptake of L-aspartate in aerobic conditions is coupled to the excretion of fumarate, resulting in the net uptake of nitrogen without carbon uptake. In addition, during anaerobic growth, catalyzes the uptake of fumarate, malate or aspartate coupled to the export of succinate. May play a a general role in anaerobic C4-dicarboxylate transport.
P40684
Q5GFD9
IMPCT_RAT
Imprinted and ancient gene protein homolog
Rattus
MAEVESGSNQRQNEEIEAMAAIYGEEWCVIDEVAKIFCIRITDDMDDPKWTLCLQVMLPSEYPGTAPPVYQLNAPWLKGQERAELAKSLEEIYMKNIGESILYQWVEKIRDALIQKSQITEPGPDEKKKTEEEEVEGEDDPILEHPPENPVKTWDLKISESAPEAEELPPIAHGAPITDRRSTFQAHLAPVVCIDQVKKVLAKLYENKKIASATHNIYAYRIYCEDKQTFLQDSEDDGETAAGGRLLHLMEILNVKNVMVVVSRWYGGILLGPDRFKHINNCARNILVEKNFTNSPEESAKSFGKKKVKKDKKKGDH
Translational regulator that ensures constant high levels of translation upon a variety of stress conditions, such as amino acid starvation, UV-C irradiation, proteasome inhibitor treatment and glucose deprivation. Plays a role as a negative regulator of the EIF2AK4/GCN2 kinase activity; impairs GCN1-mediated EIF2AK4/GCN2 activation, and hence EIF2AK4/GCN2-mediated eIF-2-alpha phosphorylation and subsequent down-regulation of protein synthesis. May be required to regulate translation in specific neuronal cells under amino acid starvation conditions by preventing GCN2 activation and therefore ATF4 synthesis. Through its inhibitory action on EIF2AK4/GCN2, plays a role in differentiation of neuronal cells by stimulating neurite outgrowth.
Q5GFD9
A4Y6B8
GLO2_SHEPC
Glyoxalase II
Shewanella
MLTITAIKAFNDNYIWVLQQTPHSQVYVVDPGDAKVVIAYLVSHQLALAGILLTHHHQDHTGGVGELKRYVEQTSSQTLQVYGPQKENIAHVNVPLNPEMRTELTLPFLNAQIQVLNVPGHTAGHIAYFIEDALFCGDTLFSAGCGRLFEGTAEQMLSSLTLLAKLPANTRVFCAHEYTLSNLKFALTVEPNNLNLQAYMQKATEMRAQNSATIPSSIALERAINPFLRVGEQSIIDSIKQHFDDPDPIKLDELTCFTRLRQWKDIF
Thiolesterase that catalyzes the hydrolysis of S-D-lactoyl-glutathione to form glutathione and D-lactic acid.
A4Y6B8
Q2N908
TAL_ERYLH
Probable transaldolase
Erythrobacter
MQFFADTAEIDDIKELAATGLLDGVTTNPSLIHKSGRDFIEVTKEICGITDGPVSAEVVALDHATMMKEADKLRAIADNVCIKVPLTIDGLKTCKALSDDGTMVNVTLCFSANQALLAAKAGATFVSPFVGRHDDNGFNGMELIRDIRTIYDNYAFETEILVASVRHTTHVLEAALIGADVMTAPPKVIMALANHVLTNKGIEGFLKDWEATGQSIL
Transaldolase is important for the balance of metabolites in the pentose-phosphate pathway.
Q2N908
Q39262
ZFP3_ARATH
Zinc finger protein 3
Arabidopsis
MDASIVSSSTAFPYQDSLNQSIEDEERDVHNSSHELNLIDCIDDTTSIVNESTTSTEQKLFSCNYCQRTFYSSQALGGHQNAHKRERTLAKRGQRMAASASAFGHPYGFSPLPFHGQYNNHRSLGIQAHSISHKLSSYNGFGGHYGQINWSRLPFDQQPAIGKFPSMDNFHHHHHQMMMMAPSVNSRSNNIDSPSNTGRVLEGSPTLEQWHGDKGLLLSTSHHEEQQKLDLSLKL
Acts as negative regulator of abscisic acid (ABA) signaling during germination and early seedling development. Involved in the regulation of vegetative development and fertility. Modulates red light signaling in seedling photomorphogenesis.
Q39262
Q21252
NAS3_CAEEL
Nematode astacin 3
Caenorhabditis
MYRFIIFFSLLALTASKVSEPEKDDEIAVKIPTKRSVSEPPKDDDIAVKIPMRKKRGIAIHPWQWESHLWPNAEVPYDIASHYTATERGIILSAMEAFRDVTCVRFRPRRSTDKHYLQINKHYQLERCFSYIGRQSSRWLFGTRDGKVETRMKLDPSCLLYNGRGTVMHELMHILGFYHEHQRDDRDRRIGGSASHYNFKIYQRAKSYYMGGYDANSIMHYNFGSVPWQKRDYFSPSDIRNINTLYKCNNRVVSKFPSTIPSTSTTTTKAPQFELFEKKQIESNSLFRRRRS
Metalloprotease.
Q21252
Q7VYU0
CRCB_BORPE
Putative fluoride ion transporter CrcB
Bordetella
MLTYAPLNFIAIGIGATLGAWLRWVLGLRLNGAGWPWGTLTANLVGGYLIGVMVALIASHPEWPAWIRLAAVTGFLGGLTTFSTFSAETVDMLERGVYATAAAYAGASLAGSLAMTGLGLATVRLLLR
Important for reducing fluoride concentration in the cell, thus reducing its toxicity.
Q7VYU0
Q753K4
SYF2_ASHGO
Pre-mRNA-splicing factor SYF2
Eremothecium
MGIEDINRRLRQLKKKRVDASIRNRKEAASEERARLAEGKPRVYSMAEEPADEAEADDTQSEQLKLLNYRIADYEKWDEKQKRHKQPSDGADLGELANSTYRSELHQLHRRGVVKGRATNGRISASGKVVLDDEPELVEKLAAAVQQTAKRRHEERQKKAAKDGGRATAGSLNDKNRHFNEKLDREFRKRGQ
Involved in pre-mRNA splicing.
Q753K4
B1GZ94
RL24_ENDTX
50S ribosomal protein L24
Endomicrobium
MLNIKKKDKVLILSGKDRGKKGEVIYVSPDKGKVIVTKINVVKRHTNPTRKDLGGIHKKEAPIAISKIMLICPKCSRGSRAKFDKLSDGKKIRVCRRCGEVIV
One of the proteins that surrounds the polypeptide exit tunnel on the outside of the subunit.
B1GZ94
Q6F7S4
RL5_ACIAD
50S ribosomal protein L5
Acinetobacter
MARLKTRYNEELKAKLQQELGIKNVMEIPRITKITLNMGVGAAATDKKLLDGAVADMQLIAGQKPVVTLARKSIAGFKIRDGWPIGCKVTLRGEQMYEFLDRLISIAIPRIRDFRGFSSKSFDGRGNYSMGLKEQIVFPEIDFDKIDRIRGMDITITTTARTDDEGRALMRTFGFPFK
This is 1 of the proteins that binds and probably mediates the attachment of the 5S RNA into the large ribosomal subunit, where it forms part of the central protuberance. In the 70S ribosome it contacts protein S13 of the 30S subunit (bridge B1b), connecting the 2 subunits; this bridge is implicated in subunit movement. Contacts the P site tRNA; the 5S rRNA and some of its associated proteins might help stabilize positioning of ribosome-bound tRNAs.
Q6F7S4
Q2NRL9
LPXA_SODGM
Acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase
Sodalis
MIDQSAFIHPSAIVEDGAIIHADVHVGPFCVIGPQVEIGARTVLESHVVVTGITRIGEDNQIYPFASLGDVNQDLKYAGEPTRVEIGHRNRIRESVTIHRGTIQGGEVTRVGSDNLLMVNAHVAHDCTVGSHCIMANNATLGGHVAVDDYAIIGGMTAVHQFCVIGAYVMVGGCSGVAQDVPPFVIAQGNHATPFGLNIEGLKRRGFDHAALHAIRAAYKIIYRSGKTLDEAKPELQALAQEHQVVNTFLDFLLRSQRGIIR
Involved in the biosynthesis of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell.
Q2NRL9
Q5V0E6
QUEC_HALMA
PreQ(0) synthase
Haloarcula
MTDDTRAVVLASGGMDSATAAYEAQTRGYDHLYLLHTSYGQNTEDREYECASALADHVDAADFLHVETGHLTQIGASSLTDDSMEVADADTDSDEIPTSYVPFRNANLLSMAVSYAEANDCGAVFIGAHSEDFSGYPDCRPAFFDAFQGVIDAGTKPDTDIALVAPFVEWSKTDIAERGVELGVPYADTWSCYRDDEPACGTCDACAFRLEAFQRIGERDPIEYAERPTYAE
Catalyzes the ATP-dependent conversion of 7-carboxy-7-deazaguanine (CDG) to 7-cyano-7-deazaguanine (preQ(0)).
Q5V0E6
B5EFQ9
RS17_CITBB
30S ribosomal protein S17
Citrifermentans
MSERGNRKTQVGVVVSDKMDKTAVVKVDRLVKHPVYNKYIKRSAKYKAHDMDNAAKIGDRVLIVETRPLSKDKRWKIRQIIESKG
One of the primary rRNA binding proteins, it binds specifically to the 5'-end of 16S ribosomal RNA.
B5EFQ9
B1J5G5
MTNA_PSEPW
S-methyl-5-thioribose-1-phosphate isomerase
Pseudomonas
MRERLMAAEKVTGIRWHHGALHLLDQRLLPSQERWLACDNVAQVAAAIRDMAVRGAAAIGIAAAYGLVLALEERLAEGGDWEMDLEEDFLSLAEARPTAANLFWALNRMRDRLQRLRPGEDVLAALEAEAVAIHESDREANLTMAQQGIELIRRHQGSEQALLTYGNAGALASGGFGTALGVIRAGFLEGMVERVYAGETRPWLQGSRLTAWELANEGIPVTLCADSALAHLMKSKGITWVVVGADCIAANGDVASKIGTYQLAVNAMHHGVRFMVVAPSTSIDLNLATGEDIPLEERDADELLDYAGTRVAPQVEVFNPVFDVTPADLIDVIVTEKGVIERPDTAKLAQLMCRKRLH
Catalyzes the interconversion of methylthioribose-1-phosphate (MTR-1-P) into methylthioribulose-1-phosphate (MTRu-1-P).
B1J5G5
O51742
RBFA_BORBU
Ribosome-binding factor A
Borreliella
MYKNIKKFKLESFIAQEIGNLIVSGGIKDPRIHSFLTVVKVEFSKDLINAKVFMGSIKEGASLDNAVKALNNAKGFIQSQIIKRIKVRSTPKLLFVKDDSLSKSFYVNKLIEGLNTTREN
One of several proteins that assist in the late maturation steps of the functional core of the 30S ribosomal subunit. Associates with free 30S ribosomal subunits (but not with 30S subunits that are part of 70S ribosomes or polysomes). Required for efficient processing of 16S rRNA. May interact with the 5'-terminal helix region of 16S rRNA.
O51742
Q59RL7
CPH2_CANAL
Candida pseudohyphal regulator 2
Candida
MLSQYDEQLAAGDNNGFNKQGNATLYSFDFVDADDFLDSISGALPNNGHNNVNPNTNDISFEDMNIMNPNIYSPVSAASGDDFTQSSGQPMISEGSNYTGQNFTDYLSDNSLEGYDKNTSRPLHEVDIGFSNKRSNSTSTGSLSHNEEITPISHYSVDSIVTSPEPPINKQGDFPPIKRTTTVSSTNSITNTTKKPAKVTKPKSKDKNSHNMIEKKYRTNINTKILALRDAVPALRIAAGCDDVSIADLEGLTPASKLNKASVLTKATEYIKHLESKNFILKQQNIELHRLIQHANMNPKSLPPPPQQMQAPPQPGFGFYPPQNQSFNVTPASQYPSPQQQVSPTQQQTVHHPPQPNRYLLGGMAAVMGTSLFGGSGENDFRSLSALPFSYLFPNAILNPSPLTIQLWTLTKVLLVVGSLASIFIPMYKQAQLKKEDKPNTIPETSLLDWILISIGFKTPAKLSVSKRDAIISNLQGGNDWSQLVSDYFYLAGCEINFENCFLSLVLGTIIRHRFPVVATILNHYLSMKEALLLNLDYKGFSKSLIRLNQLISKVDGVSIFESTNLTTRLTNVFTNNRINANIVDGQNHVKYIEFYQRNINDYYAIVFNWRLLEFIHELNVTYLEQLNDDQSQVLTDLKIIEAFFGEQDNKLFGYYQLFTSILNANYAPYLFESLKDKVESSLEKFRIAYEGIDLTDHEIHNTSSEDEYEQESPVVYKYEPTLKSQKSLISSLNLVNEEEFIILTCSLTIYYYKNKEYDRALKLLNYLRLDNDSKTLSLLTFTSLITLINELIPGKIEDNVNLDSAIRICRDWLENPDLTQYMDEDIKLELKKIVVTKGMIVNGIDVNESDEE
Transcription factor that positively controls filamentous growth, virulence, and invasiveness. Binds directly to the two SRE-1-like elements upstream of TEC1 and thus regulates positively expression of this important hyphal growth regulator. Functions independently of known signaling cascades involving EFG1. Regulates also gene expression during intestinal colonization but is not involved in host cell adhesion.
Q59RL7
Q8VW75
COAD_PHODP
Pantetheine-phosphate adenylyltransferase
Photobacterium
MTTRVIYPGTFDPITNGHLDLIERAAAMFDTVIVGVAYNPTKKPLFDLNERVALAQSVTQHLPNVEIVGFSGLLVNFAKEHNANVLVRGLRAVSDFEYEFQLANMNRRLMPELETVFLTPAEENSFISSTIVKEVALHKGDVSQFVPNQISQALNKKLFA
Reversibly transfers an adenylyl group from ATP to 4'-phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate.
Q8VW75
B9I2J6
AXEP_POPTR
L-Ala-D/L-Xxx epimerase
Populus
MLSIGSLCLSLGTTPKPLKPSKTPKPIRKLYATKAMAGSNPKQVSTFEFRDLMETFAVDVKRAENRPLNVPLIAPFTIASSRLDKVENVAIRIELSDGCVGWGEAPILPFVTAEDQSTAMIKAREACELLKNSSSMKLGLVLERVSEILPGHEFASVRAGVEMALIDAVAKSINVPLWILFGGASDSITTDITIPIVSSAEAAELASKYRKQGFQTLKLKVGKNLKEDIEVLQAIRAVHPDCLFILDANEGYKPEEAIEVLEELHKMGVTPILFEQPVHRDDWEGLGHVTHIAKGKYGVSVAADESCRSLVDAKRIIKGNLADVINIKLAKVGVVGGLEIIEEARTSGLDLMIGGMVETRLAMGFAGHLAAGFGCFKFIDLDTPLLLSEDPVLEGYEVSGAVYKFTDAQGHAGFLDWDNVL
Catalyzes the epimerization of various hydrophobic and polar dipeptides. Has epimerase activity with L-Ala-L-Ala, L-Ala-L-Ser, L-Ala-L-Thr and L-Ala-L-Trp (in vitro).
B9I2J6
B3VMC0
BADH2_ORYSI
Betaine aldehyde dehydrogenase 2
Oryza sativa
MATAIPQRQLFVAGEWRAPALGRRLPVVNPATESPIGEIPAGTAEDVDAAVAAAREALKRNRGRDWARAPGAVRAKYLRAIAAKIIERKSELARLETLDCGKPLDEAAWDMDDVAGCFEYFADLAESLDKRQNAPVSLPMENFKCYLRKEPIGVVGLITPWNYPLLMATWKVAPALAAGCTAVLKPSELASVTCLELADVCKEVGLPSGVLNIVTGLGSEAGAPLSSHPGVDKVAFTGSYETGKKIMASAAPMVKPVSLELGGKSPIVVFDDVDVEKAVEWTLFGCFWTNGQICSATSRLILHKKIAKEFQERMVAWAKNIKVSDPLEEGCRLGPVVSEGQYEKIKQFVSTAKSQGATILTGGVRPKHLEKGFYIEPTIITDVDTSMQIWREEVFGPVLCVKEFSTEEEAIELANDTHYGLAGAVLSGDRERCQRLTEEIDAGIIWVNCSQPCFCQAPWGGNKRSGFGRELGEGGIDNYLSVKQVTEYASDEPWGWYKSPSKL
Dehydrogenase that can use N-acetyl-c-aminobutyraldehyde (NAGABald), gamma-guanidinobutyraldehyde (GGBald), betaine aldehyde (Bet-ald), gamma-aminobutyraldehyde (GAB-ald), acetaldehyde, 4-aminobutylaldehyde (AB-ald), 3-aminopropionaldehyde (AP-ald), 4-N-trimethylaminobutyraldehyde (TMAB-ald) and 3-N-trimethylaminopropionaldehyde (TMAP-ald) as substrates. Catalyzes the oxidation of GAB-ald more efficiently than Bet-ald. Mediates the conversion of GAB-ald into gamma-aminobutyric acid (GABA), and prevents the formation of 2-acetyl-1-pyrroline (2AP) which gives fragrant rice its aromatic properties.
B3VMC0
B7J440
NRDR_ACIF2
Transcriptional repressor NrdR
Acidithiobacillus
MHCPFCAYADTRVVDSRLADDGGSVRRRRECPQCGQRFTTFERAELALPVVVKTDGRRESFNEEKLQRGLTRALSKRPVATARVDAAVRMIQRRIRERGEREIPARLIGELVMEALRDLDPVAYVRFASVYRRFEDVDAFSVEIARMKEAEVPDGGDDLNRGD
Negatively regulates transcription of bacterial ribonucleotide reductase nrd genes and operons by binding to NrdR-boxes.
B7J440
Q9WY79
MURE_THEMA
UDP-N-acetylmuramyl-tripeptide synthetase
Thermotoga
MNISTIVSNLKDLILEVRAPYDLEITGVSNHSSKVKKGDLFICRRGEKFDSHEIIPEVMEKGAVAVVVEREIDLDFPYIQVFDSRYFEAKVASLFFEDPWKDVLTFGVTGTNGKTTTTMMIYHMLTSLGERGSVLTTAVKRILGNSYYDDITTPDAITILSAMKENREGGGKFFALEVSSHALVQQRVEGVRFDVGIFTNISRDHLDFHGTFENYLKAKLHLFDLLKDDGVAVLNESLADAFNRKSRKITFGTSKNADYRLGNIEVSWEGTQFVLETPDGLLKVFTRAIGDFNAYNAAAAIAALHQLGYDPKDLASSLETFTGVEGRFEVVRGAKKIGLNVVVDFAHSPDALEKLLKNVRKISQGRVIVVFGAGGNSDRGKRPMMSEVASKLADVVILTTDDPRGEDPEQIMEDLIKGIDKRKPYLVLFDRREAIETALTIANRGDSVVIAGRGHERYQIIDEEKKVPFQDREVVEEIIRDKLKGRKYAQ
Catalyzes the addition of both L- and D-lysine to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanyl-D-glutamate (UMAG) in the biosynthesis of bacterial cell-wall peptidoglycan. Is also able to use meso-diaminopimelate as the amino acid substrate in vitro, although much less efficiently.
Q9WY79
B2SCZ4
CH60_BRUA1
Chaperonin-60
Brucella
MAAKDVKFGRTAREKMLRGVDILADAVKVTLGPKGRNVVIEKSFGAPRITKDGVSVAKEVELEDKFENMGAQMLREVASKTNDTAGDGTTTATVLGQAIVQEGAKAVAAGMNPMDLKRGIDLAVNEVVAELLKKAKKINTSEEVAQVGTISANGEAEIGKMIAEAMQKVGNEGVITVEEAKTAETELEVVEGMQFDRGYLSPYFVTNPEKMVADLEDAYILLHEKKLSNLQALLPVLEAVVQTSKPLLIIAEDVEGEALATLVVNKLRGGLKIAAVKAPGFGDRRKAMLEDIAILTGGQVISEDLGIKLESVTLDMLGRAKKVSISKENTTIVDGAGQKAEIDARVGQIKQQIEETTSDYDREKLQERLAKLAGGVAVIRVGGATEVEVKEKKDRVDDALNATRAAVEEGIVAGGGTALLRASTKITAKGVNADQEAGINIVRRAIQAPARQITTNAGEEASVIVGKILENTSETFGYNTANGEYGDLISLGIVDPVKVVRTALQNAASVAGLLITTEAMIAELPKKDAAPAGMPGGMGGMGGMDF
Together with its co-chaperonin GroES, plays an essential role in assisting protein folding. The GroEL-GroES system forms a nano-cage that allows encapsulation of the non-native substrate proteins and provides a physical environment optimized to promote and accelerate protein folding.
B2SCZ4
P26350
PTMA_MOUSE
Thymosin alpha
Mus
MSDAAVDTSSEITTKDLKEKKEVVEEAENGRDAPANGNAQNEENGEQEADNEVDEEEEEGGEEEEEEEEGDGEEEDGDEDEEAEAPTGKRVAEDDEDDDVDTKKQKTEEDD
Prothymosin alpha may mediate immune function by conferring resistance to certain opportunistic infections.
P26350
Q1E0G9
EFG1P_COCIM
rRNA-processing protein EFG1
Coccidioides
MSLHEPEAQPSLKKRRRDSFSNADPKRVKRLHSGTQRLHYHDIGPSVNELKTRIRDVKRLLAKRIDDLPADVRVAKERELAECQRDLEKAEVKKQRSKMIQKYHFVRFLERKRATKELKRLKGQLHKLENDDRLDPNARENSIETLNRKISASEIDLNYTIYSPLTEKYISLYPNERRKQQPMEPEESNVIRTNSGEKPPLWYTVKQSMADGTLELLRDGKLGIGLSGEKKDSNNADVSLKSNTMSLLVHRKQKKPKSKIKVDGDEDAKRSSARSVQEGTRNENKRTSKEDVQGEDDDAESESDGGFFE
Involved in rRNA processing.
Q1E0G9
Q82IY7
PTLD_STRAW
Neopentalenolactone biosynthesis protein D
Streptomyces
MSRAMDITRIPGSAIGAVVAGADFSGTIDDTQVEEIWQALDQHLVLVFRGHKDPSNDDLLMFARRFGHVPKTGLTTGASPDHNEILLISNILDENGQKIGVGNAEWMDWHTDYSFRPRVSRIGFLAAVELPPSGGGQTLFTDMYTAYESLPDDLRQRLHSYRARHSLRSGYEDVIEEEYQGEVSIEGPTAKPFVAPEDGTATVHQLIARNPRTGRRAVYANPLNTKRILELDVTSSKEVLQQLFAKPGEPELTYAHEWLPGDIVMWDQLGTVHAKRAFDPTERRLLRKVVTIFDDPAEPWHPEDAA
Catalyzes the Fe(2+) and alpha-ketoglutarate-dependent oxidation of pentalenolactone D to pentalenolactone F. Also able to catalyze the oxidation of pentalenolactone D to pentalenolactone E. In presence of neopentalenolactone D, mediates production of PL308 and possibly neopentalenolactone E.
Q82IY7